|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
515-991 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 801.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 515 LPTTALLTAGKP--TKARTEANDRIIEAITDVFEEFKVNAQVTGFSRGPTVTRYEIELGPGVKVSKITNLQSNLAYAVAT 592
Cdd:COG1674 137 LPPLDLLDPPPPkkEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 593 DNLRLLTPIPGKSAVGIEVPNADREMVRLRDVLDSPAIASDEDPMLIGLGKDIEGEYSSYSVQKMPHLLVAGATGSGKSA 672
Cdd:COG1674 217 KSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 673 FVNSMLVSLLTRATPEQVRLILVDPKMVELTPYEGIPHLITPIITQPKKAAAALQWLVEEMEQRYMDMKAARVRKIEDYN 752
Cdd:COG1674 297 CINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYN 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 753 RKVISGAHQAPlgSEREMRPYPYIVCVVDELADLMMTAPKEIEESIVRITQKARAAGIHLVLATQRPSVDVVTGLIKTNV 832
Cdd:COG1674 377 EKVREAKAKGE--EEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANI 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 833 PSRLAFATSSLTDSRVILDQGGAEKLIGMGDGLFIPQG-GRPVRMQGAFVSDEEVQAVVDAAKAQGQPNYTEGVTeekKS 911
Cdd:COG1674 455 PSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGaSKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEIL---EE 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 912 EAKKEIDDDIGKDMDDLLEAVELVVTSQLGSTSMLQRKLRIGFAKAGRLMDLMESRGVVGPSEGSKAREVLVKPEELDTI 991
Cdd:COG1674 532 EEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
515-985 |
8.31e-141 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 456.85 E-value: 8.31e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 515 LPTTALLTagkPTKARTEAND--------RIIEAitdVFEEFKVNAQVTGFSRGPTVTRYEIELGPGVKVSKITNLQSNL 586
Cdd:PRK10263 866 LPSLDLLT---PPPSEVEPVDtfaleqmaRLVEA---RLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDL 939
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 587 AYAVATDNLRLLTPIPGKSAVGIEVPNADREMVRLRDVLDSPAIASDEDPMLIGLGKDIEGEYSSYSVQKMPHLLVAGAT 666
Cdd:PRK10263 940 ARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTT 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 667 GSGKSAFVNSMLVSLLTRATPEQVRLILVDPKMVELTPYEGIPHLITPIITQPKKAAAALQWLVEEMEQRYMDMKAARVR 746
Cdd:PRK10263 1020 GSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVR 1099
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 747 KIEDYNRKVISGAHQA---------PLGSEREMRP----YPYIVCVVDELADLMMTAPKEIEESIVRITQKARAAGIHLV 813
Cdd:PRK10263 1100 NLAGYNEKIAEADRMMrpipdpywkPGDSMDAQHPvlkkEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLV 1179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 814 LATQRPSVDVVTGLIKTNVPSRLAFATSSLTDSRVILDQGGAEKLIGMGDGLFI-PQGGRPVRMQGAFVSDEEVQAVVDA 892
Cdd:PRK10263 1180 LATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSgPNSTLPVRVHGAFVRDQEVHAVVQD 1259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 893 AKAQGQPNYTEGVTEEKKSEAKKEIDDDIGKDMDDLLEAVELVVTSQLGSTSMLQRKLRIGFAKAGRLMDLMESRGVVGP 972
Cdd:PRK10263 1260 WKARGRPQYVDGITSDSESEGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSE 1339
|
490
....*....|...
gi 1004391105 973 SEGSKAREVLVKP 985
Cdd:PRK10263 1340 QGHNGNREVLAPP 1352
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
621-820 |
5.21e-64 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 215.70 E-value: 5.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 621 LRDVLDSPAIASDEDPMLIGLGKDIEGEYSSYSVQKMP-HLLVAGATGSGKSAFVNSMLVSLLTRATPEQVRLILVDPKM 699
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 700 VELTPYEGIPHLIT-PIITQPKKAAAALQWLVEEMEQRYMDMKAARVRKIEDYNRKV-------------ISGAHQAPLG 765
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIaedpldgfgdvflVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1004391105 766 SEREMRPYPYIVCVVDELADLMMTAPKE----IEESIVRITQKARAAGIHLVLATQRPS 820
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
930-984 |
5.32e-24 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 95.94 E-value: 5.32e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1004391105 930 EAVELVVTSQLGSTSMLQRKLRIGFAKAGRLMDLMESRGVVGPSEGSKAREVLVK 984
Cdd:smart00843 9 EAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
658-882 |
1.54e-23 |
|
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274858 [Multi-domain] Cd Length: 658 Bit Score: 106.98 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 658 PHLLVAGATGSGKSAFVNSMLVSLLTRATPEQVRLILVDPKMvELT--PYEGIPHlITPIITQPKKAAAalqwLVE---- 731
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKG-GATflGLEGLPH-VSAVITNLADEAP----LVDrmqd 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 732 ----EMEQRYMDMKAA-RVRKIEDYNRKVISGAHQAPLgseremrpyPYIVCVVDELADLmMTAPKEIEESIVRITQKAR 806
Cdd:TIGR03924 510 alagEMNRRQELLRAAgNFANVAEYEKARAAGADLPPL---------PALFVVVDEFSEL-LSQHPDFADLFVAIGRLGR 579
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1004391105 807 AAGIHLVLATQRPSVDVVTGLiKTNVPSRLAFATSSLTDSRVILDQGGAEKLIGM-GDGLFIPQGGRPVRMQGAFVS 882
Cdd:TIGR03924 580 SLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTpGAGYLKVDTAEPVRFRAAYVS 655
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
659-840 |
1.10e-06 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 49.14 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 659 HLLVAGATGSGKSAFVNSMLVSLLTRatpeQVRLILVDPKM---VELTPYEGIPHLITPIITqpkkaaAALQWLVEEMeq 735
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAAR----GGSVIITDPKGelfLVIPDRDDSFAALRALFF------NQLFRALTEL-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 736 rymdmkaarvrkiedynrkvisgahqaplGSEREMRPYPYIVCVVDELADLMmtapkeIEESIVRITQKARAAGIHLVLA 815
Cdd:cd01127 69 -----------------------------ASLSPGRLPRRVWFILDEFANLG------RIPNLPNLLATGRKRGISVVLI 113
|
170 180 190
....*....|....*....|....*....|.
gi 1004391105 816 TQ------RPSVDVVTGLIKTNVPSRLAFAT 840
Cdd:cd01127 114 LQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
112-240 |
3.93e-05 |
|
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.
Pssm-ID: 463896 Cd Length: 171 Bit Score: 45.27 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 112 VGVIGAYLTDAVRYVIGAGAYVLPVALIALAMALMMGVSgvagrLQPRVMGGIGLIIvsMLGLIHIFAGLPKLSWRDNAA 191
Cdd:pfam13491 47 GGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLFRRRS-----LERRWLRLLGFLL--LLLASSALFALRLPSLEFGLP 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1004391105 192 GDAGGAIGFAVGQLLEAAFSAYVAVPLLILLIIYGALNVTGITLRQAFD 240
Cdd:pfam13491 120 GGAGGVIGRLLANALVTLLGFTGATLLLLALLAIGLSLVTGFSWLALAE 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
515-991 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 801.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 515 LPTTALLTAGKP--TKARTEANDRIIEAITDVFEEFKVNAQVTGFSRGPTVTRYEIELGPGVKVSKITNLQSNLAYAVAT 592
Cdd:COG1674 137 LPPLDLLDPPPPkkEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 593 DNLRLLTPIPGKSAVGIEVPNADREMVRLRDVLDSPAIASDEDPMLIGLGKDIEGEYSSYSVQKMPHLLVAGATGSGKSA 672
Cdd:COG1674 217 KSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 673 FVNSMLVSLLTRATPEQVRLILVDPKMVELTPYEGIPHLITPIITQPKKAAAALQWLVEEMEQRYMDMKAARVRKIEDYN 752
Cdd:COG1674 297 CINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYN 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 753 RKVISGAHQAPlgSEREMRPYPYIVCVVDELADLMMTAPKEIEESIVRITQKARAAGIHLVLATQRPSVDVVTGLIKTNV 832
Cdd:COG1674 377 EKVREAKAKGE--EEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANI 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 833 PSRLAFATSSLTDSRVILDQGGAEKLIGMGDGLFIPQG-GRPVRMQGAFVSDEEVQAVVDAAKAQGQPNYTEGVTeekKS 911
Cdd:COG1674 455 PSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGaSKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEIL---EE 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 912 EAKKEIDDDIGKDMDDLLEAVELVVTSQLGSTSMLQRKLRIGFAKAGRLMDLMESRGVVGPSEGSKAREVLVKPEELDTI 991
Cdd:COG1674 532 EEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
515-985 |
8.31e-141 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 456.85 E-value: 8.31e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 515 LPTTALLTagkPTKARTEAND--------RIIEAitdVFEEFKVNAQVTGFSRGPTVTRYEIELGPGVKVSKITNLQSNL 586
Cdd:PRK10263 866 LPSLDLLT---PPPSEVEPVDtfaleqmaRLVEA---RLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDL 939
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 587 AYAVATDNLRLLTPIPGKSAVGIEVPNADREMVRLRDVLDSPAIASDEDPMLIGLGKDIEGEYSSYSVQKMPHLLVAGAT 666
Cdd:PRK10263 940 ARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTT 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 667 GSGKSAFVNSMLVSLLTRATPEQVRLILVDPKMVELTPYEGIPHLITPIITQPKKAAAALQWLVEEMEQRYMDMKAARVR 746
Cdd:PRK10263 1020 GSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVR 1099
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 747 KIEDYNRKVISGAHQA---------PLGSEREMRP----YPYIVCVVDELADLMMTAPKEIEESIVRITQKARAAGIHLV 813
Cdd:PRK10263 1100 NLAGYNEKIAEADRMMrpipdpywkPGDSMDAQHPvlkkEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLV 1179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 814 LATQRPSVDVVTGLIKTNVPSRLAFATSSLTDSRVILDQGGAEKLIGMGDGLFI-PQGGRPVRMQGAFVSDEEVQAVVDA 892
Cdd:PRK10263 1180 LATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSgPNSTLPVRVHGAFVRDQEVHAVVQD 1259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 893 AKAQGQPNYTEGVTEEKKSEAKKEIDDDIGKDMDDLLEAVELVVTSQLGSTSMLQRKLRIGFAKAGRLMDLMESRGVVGP 972
Cdd:PRK10263 1260 WKARGRPQYVDGITSDSESEGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSE 1339
|
490
....*....|...
gi 1004391105 973 SEGSKAREVLVKP 985
Cdd:PRK10263 1340 QGHNGNREVLAPP 1352
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
621-820 |
5.21e-64 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 215.70 E-value: 5.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 621 LRDVLDSPAIASDEDPMLIGLGKDIEGEYSSYSVQKMP-HLLVAGATGSGKSAFVNSMLVSLLTRATPEQVRLILVDPKM 699
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 700 VELTPYEGIPHLIT-PIITQPKKAAAALQWLVEEMEQRYMDMKAARVRKIEDYNRKV-------------ISGAHQAPLG 765
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIaedpldgfgdvflVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1004391105 766 SEREMRPYPYIVCVVDELADLMMTAPKE----IEESIVRITQKARAAGIHLVLATQRPS 820
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
515-613 |
3.26e-34 |
|
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. FtsK can be split into three domains called alpha (this entry), beta and gamma. The alpha and beta domains contain the core ATPase machinery of the DNA translocase.
Pssm-ID: 436096 [Multi-domain] Cd Length: 101 Bit Score: 126.50 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 515 LPTTALLTAGKP--TKARTEANDRIIEAITDVFEEFKVNAQVTGFSRGPTVTRYEIELGPGVKVSKITNLQSNLAYAVAT 592
Cdd:pfam17854 1 LPPLDLLEPPPTssQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 1004391105 593 DNLRLLTPIPGKSAVGIEVPN 613
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
930-984 |
1.70e-25 |
|
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix structure. Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 462786 [Multi-domain] Cd Length: 63 Bit Score: 100.14 E-value: 1.70e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1004391105 930 EAVELVVTSQLGSTSMLQRKLRIGFAKAGRLMDLMESRGVVGPSEGSKAREVLVK 984
Cdd:pfam09397 9 EAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
930-984 |
5.32e-24 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 95.94 E-value: 5.32e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1004391105 930 EAVELVVTSQLGSTSMLQRKLRIGFAKAGRLMDLMESRGVVGPSEGSKAREVLVK 984
Cdd:smart00843 9 EAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
658-882 |
1.54e-23 |
|
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274858 [Multi-domain] Cd Length: 658 Bit Score: 106.98 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 658 PHLLVAGATGSGKSAFVNSMLVSLLTRATPEQVRLILVDPKMvELT--PYEGIPHlITPIITQPKKAAAalqwLVE---- 731
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKG-GATflGLEGLPH-VSAVITNLADEAP----LVDrmqd 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 732 ----EMEQRYMDMKAA-RVRKIEDYNRKVISGAHQAPLgseremrpyPYIVCVVDELADLmMTAPKEIEESIVRITQKAR 806
Cdd:TIGR03924 510 alagEMNRRQELLRAAgNFANVAEYEKARAAGADLPPL---------PALFVVVDEFSEL-LSQHPDFADLFVAIGRLGR 579
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1004391105 807 AAGIHLVLATQRPSVDVVTGLiKTNVPSRLAFATSSLTDSRVILDQGGAEKLIGM-GDGLFIPQGGRPVRMQGAFVS 882
Cdd:TIGR03924 580 SLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTpGAGYLKVDTAEPVRFRAAYVS 655
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
658-850 |
3.48e-20 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 96.98 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 658 PHLLVAGATGSGKSAFVNSMLVSLLTRATPEQVRLILVDPK---MVEltPYEGIPHLITPII----TQPKKAAAALQwlv 730
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMAN--LFKNLPHLLGTITnldgAQSMRALASIK--- 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 731 EEMEQRYMDMKAARVRKIEDYNRKVISGAHQAPLgseremrpyPYIVCVVDELADLMMTAPKEIEE--SIVRItqkARAA 808
Cdd:TIGR03928 545 AELKKRQRLFGENNVNHINQYQKLYKQGKAKEPM---------PHLFLISDEFAELKSEQPEFMKElvSTARI---GRSL 612
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1004391105 809 GIHLVLATQRPSvDVVTGLIKTNVPSRLAFATSSLTDSRVIL 850
Cdd:TIGR03928 613 GVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
651-892 |
1.51e-12 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 72.33 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 651 SYSVQKMPHLLVAGATGSGKSAFVNSMLVSLLTRATPEQVRLILVDPKMVELTPYEGIPHlITPIIT--QPKKAAAALQW 728
Cdd:TIGR03928 804 TLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTldEEEKIEKLIRR 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 729 LVEEMEQRYMDMKAARVRKIEDYNRKvisgahqaplgSEREMrpyPYIVCVVDELaDLMMTAP--KEIEESIVRITQKAR 806
Cdd:TIGR03928 883 IKKEIDRRKKLFSEYGVASISMYNKA-----------SGEKL---PQIVIIIDNY-DAVKEEPfyEDFEELLIQLAREGA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 807 AAGIHLVL-ATQRPSVDVVtglIKTNVPSRLAFATSSLTDSRVILdqgGAEKL---------IGMGDGLFIPQGGRPVRM 876
Cdd:TIGR03928 948 SLGIYLVMtAGRQNAVRMP---LMNNIKTKIALYLIDKSEYRSIV---GRTKFtieeipgrgLIKKDEPTLFQTALPVKG 1021
|
250
....*....|....*.
gi 1004391105 877 QGAFVSDEEVQAVVDA 892
Cdd:TIGR03928 1022 EDDLEVIENIKAEIQK 1037
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
639-877 |
1.29e-11 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 69.25 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 639 IGLGKDIEG-EYSSYSVQKMPHLLVAGATGSGKSAFVNSMLVSLltrATPEQVRLILVDPKMVELTPYEGIPHLITpIIT 717
Cdd:TIGR03928 1077 IPIGLDEETvEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTL---AKQEKEKIGLIDSIDRGLLAYRDLKEVAT-YIE 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 718 QPKKAAAALQWLVEEMEQRYMDMKAARvrkiedynrkvisgahqaplGSEREMRPYPYIVCVVDELADLMMTAPKEIEES 797
Cdd:TIGR03928 1153 EKEDLKEILAELKEEIELREAAYKEAL--------------------QNETGEPAFKPILLIIDDLEDFIQRTDLEIQDI 1212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 798 IVRITQKARAAGIHLVLATQRPSV----DVVTGLIKTnvpSRLAFATSSLTDSRVI-LDQGGAEKLIGMGDGLFIpQGGR 872
Cdd:TIGR03928 1213 LALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ---LRTGILGMRKSDQSFFkLPFTRSEKELEPGEGYFV-VNGK 1288
|
....*
gi 1004391105 873 PVRMQ 877
Cdd:TIGR03928 1289 YQKIK 1293
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
659-848 |
9.44e-07 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 52.69 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 659 HLLVAGATGSGKSAFVNSMLVSLLTRATPEQVRLILVDPKMVELTPYEGIPHlITPIITQ--PKKAAAALQWLVEEMEQR 736
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH-VGGVAGRldPERVRRTVAEVEGLLRRR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 737 YMDMKAARVRKIEDYNRkvisgAHQAPLGSEremRPYPYIVCVVDELADLmMTAPKEIEESIVRITQKARAAGIHLVLAT 816
Cdd:TIGR03925 160 ERLFRTHGIDSMAQYRA-----RRAAGRLPE---DPFGDVFLVIDGWGTL-RQDFEDLEDKVTDLAARGLAYGVHVVLTA 230
|
170 180 190
....*....|....*....|....*....|....*...
gi 1004391105 817 -----QRPSV-DVVTGLIKTnvpsRLAFATSSLTDSRV 848
Cdd:TIGR03925 231 srwseIRPALrDLIGTRIEL----RLGDPMDSEIDRRA 264
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
659-840 |
1.10e-06 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 49.14 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 659 HLLVAGATGSGKSAFVNSMLVSLLTRatpeQVRLILVDPKM---VELTPYEGIPHLITPIITqpkkaaAALQWLVEEMeq 735
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAAR----GGSVIITDPKGelfLVIPDRDDSFAALRALFF------NQLFRALTEL-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 736 rymdmkaarvrkiedynrkvisgahqaplGSEREMRPYPYIVCVVDELADLMmtapkeIEESIVRITQKARAAGIHLVLA 815
Cdd:cd01127 69 -----------------------------ASLSPGRLPRRVWFILDEFANLG------RIPNLPNLLATGRKRGISVVLI 113
|
170 180 190
....*....|....*....|....*....|.
gi 1004391105 816 TQ------RPSVDVVTGLIKTNVPSRLAFAT 840
Cdd:cd01127 114 LQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
658-815 |
6.23e-06 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 49.99 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 658 PHLLVAGATGSGKSAFVNSMLVSLLTRATPEQVRLILVDPK--MVELTPYEgipHLITPIITQPKKAAAALQwLVEEMEQ 735
Cdd:TIGR03925 364 PHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRrtLLGAVPED---YLAGYAATSAALTELIAA-LAALLER 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 736 RY--MDMKAARVRkiedyNRKVISGahqaplgseremrpyPYIVCVVDELaDLMMTAPKEIEESIVRITQKARAAGIHLV 813
Cdd:TIGR03925 440 RLpgPDVTPQQLR-----ARSWWSG---------------PEIYVVVDDY-DLVATGSGNPLAPLVELLPHARDIGLHVV 498
|
..
gi 1004391105 814 LA 815
Cdd:TIGR03925 499 VA 500
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
619-820 |
2.27e-05 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 48.06 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 619 VRLRDVLDSPAIASDEDPMLIGLGKDIEGEYSsYSVQKM--PHLLVAGATGSGKSAFVNSMLVSLLTRatpeQVRLILVD 696
Cdd:COG0433 8 VYLADDEELEELLGDGGGILIGKLLSPGVPVY-LDLDKLlnRHILILGATGSGKSNTLQVLLEELSRA----GVPVLVFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 697 PK---------------MVELTPYEGIPHLITPI--------------------ITQPKKAAAALQWL------------ 729
Cdd:COG0433 83 PHgeysglaepgaeradVGVFDPGAGRPLPINPWdlfataselgplllsrldlnDTQRGVLREALRLAddkglllldlkd 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 730 -------VEEMEQRYMDMKAARVRKIEDYNRKVISGAH------------------------------------------ 760
Cdd:COG0433 163 lialleeGEELGEEYGNVSAASAGALLRRLESLESADGlfgepgldledllrtdgrvtvidlsglpeelqstfvlwllre 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004391105 761 ---QAPLGSEREMRPYPyIVCVVDELADLMMTAPKEIEESIVRITQKARAAGIHLVLATQRPS 820
Cdd:COG0433 243 lfeARPEVGDADDRKLP-LVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS 304
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
112-240 |
3.93e-05 |
|
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.
Pssm-ID: 463896 Cd Length: 171 Bit Score: 45.27 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004391105 112 VGVIGAYLTDAVRYVIGAGAYVLPVALIALAMALMMGVSgvagrLQPRVMGGIGLIIvsMLGLIHIFAGLPKLSWRDNAA 191
Cdd:pfam13491 47 GGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLFRRRS-----LERRWLRLLGFLL--LLLASSALFALRLPSLEFGLP 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1004391105 192 GDAGGAIGFAVGQLLEAAFSAYVAVPLLILLIIYGALNVTGITLRQAFD 240
Cdd:pfam13491 120 GGAGGVIGRLLANALVTLLGFTGATLLLLALLAIGLSLVTGFSWLALAE 168
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
658-697 |
5.29e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 40.70 E-value: 5.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1004391105 658 PHLLVAGATGSGKSAFVNSMLVSLLTRatpeQVRLILVDP 697
Cdd:COG3451 205 GNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
|
|
| |
